GIN_BACSU
ID GIN_BACSU Reviewed; 64 AA.
AC P37534;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Anti-sigma-G factor Gin {ECO:0000303|PubMed:18208527};
DE AltName: Full=Protein CsfB {ECO:0000303|PubMed:8759874};
GN Name=csfB {ECO:0000303|PubMed:8759874};
GN Synonyms=gin {ECO:0000303|PubMed:18208527}, yaaM;
GN OrderedLocusNames=BSU00240;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Bookstein C., Edwards C.W., Hulett F.M.;
RT "Characterization of the Bacillus subtilis xpaC gene, which in double copy
RT causes aberrant cell morphology, filamentation and inhibits sporulation.";
RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA Ogasawara N., Nakai S., Yoshikawa H.;
RT "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT chromosome containing the replication origin.";
RL DNA Res. 1:1-14(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP DEVELOPMENTAL STAGE, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / PY79;
RX PubMed=8759874; DOI=10.1128/jb.178.16.5039-5041.1996;
RA Decatur A., Losick R.;
RT "Identification of additional genes under the control of the transcription
RT factor sigma F of Bacillus subtilis.";
RL J. Bacteriol. 178:5039-5041(1996).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / BR151;
RX PubMed=17921305; DOI=10.1128/jb.01265-07;
RA Chary V.K., Xenopoulos P., Piggot P.J.;
RT "Expression of the sigmaF-directed csfB locus prevents premature appearance
RT of sigmaG activity during sporulation of Bacillus subtilis.";
RL J. Bacteriol. 189:8754-8757(2007).
RN [6]
RP FUNCTION, INTERACTION WITH SIGMA-G FACTOR, AND MUTAGENESIS OF
RP 15-ASP--ASP-32.
RC STRAIN=168 / JH642;
RX PubMed=18208527; DOI=10.1111/j.1365-2958.2008.06121.x;
RA Karmazyn-Campelli C., Rhayat L., Carballido-Lopez R., Duperrier S.,
RA Frandsen N., Stragier P.;
RT "How the early sporulation sigma factor sigmaF delays the switch to late
RT development in Bacillus subtilis.";
RL Mol. Microbiol. 67:1169-1180(2008).
RN [7]
RP FUNCTION, INTERACTION WITH SIGMA-G FACTOR, AND MUTAGENESIS OF
RP 11-CYS--CYS-14; CYS-11; CYS-14; GLY-21; 30-CYS--CYS-33; CYS-30; CYS-33;
RP TYR-47; 49-PHE-TYR-50; TYR-50 AND VAL-51.
RX PubMed=19497328; DOI=10.1016/j.jmb.2009.05.073;
RA Rhayat L., Duperrier S., Carballido-Lopez R., Pellegrini O., Stragier P.;
RT "Genetic dissection of an inhibitor of the sporulation sigma factor
RT sigma(G).";
RL J. Mol. Biol. 390:835-844(2009).
CC -!- FUNCTION: An anti-sigma-G factor, prevents premature activation of
CC sigma-G factor in the forespore; overexpression leads to 1000-fold
CC reduction in spore formation, spore formation stops after engulfment
CC (PubMed:17921305, PubMed:19497328). Overexpression also inhibits sigma-
CC G transcription activation activity (PubMed:18208527). When both Gin
CC and sigma-G are expressed in E.coli Gin inhibits sigma-G, strongly
CC suggesting Gin inhibits by direct physical interaction
CC (PubMed:19497328). {ECO:0000269|PubMed:17921305,
CC ECO:0000269|PubMed:18208527, ECO:0000269|PubMed:19497328}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:19497328};
CC Note=Binds 0.5 mol of zinc/mol protein, probably 1 zinc per dimer.
CC {ECO:0000269|PubMed:19497328};
CC -!- SUBUNIT: Probably functions as a homodimer (PubMed:19497328). Interacts
CC with sigma-G factor, recognition occurs via the first 71 residues of
CC sigma-G (PubMed:18208527, PubMed:19497328).
CC {ECO:0000269|PubMed:18208527, ECO:0000269|PubMed:19497328}.
CC -!- DEVELOPMENTAL STAGE: Expressed starting 2 hours after sporulation onset
CC for at least 7 hours. {ECO:0000269|PubMed:8759874}.
CC -!- INDUCTION: During sporulation under control of sigma-F factor.
CC {ECO:0000269|PubMed:8759874}.
CC -!- DISRUPTION PHENOTYPE: Premature expression of sigma-G factor (sigG or
CC spoIIIG) activity during the early stages of forespore development
CC (PubMed:17921305, PubMed:18208527). Spore formation continues normally
CC (PubMed:17921305, PubMed:8759874). However its absence has deleterious
CC effects on strain robustness and is strongly selected against in
CC competitions experiments (PubMed:18208527).
CC {ECO:0000269|PubMed:17921305, ECO:0000269|PubMed:18208527,
CC ECO:0000269|PubMed:8759874}.
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DR EMBL; M96156; AAA22890.1; -; Genomic_DNA.
DR EMBL; D26185; BAA05260.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11800.1; -; Genomic_DNA.
DR PIR; S27525; S27525.
DR RefSeq; NP_387905.1; NC_000964.3.
DR RefSeq; WP_003243294.1; NZ_JNCM01000028.1.
DR PDB; 5N7Y; NMR; -; A/C=1-48.
DR PDBsum; 5N7Y; -.
DR AlphaFoldDB; P37534; -.
DR BMRB; P37534; -.
DR SMR; P37534; -.
DR STRING; 224308.BSU00240; -.
DR PaxDb; P37534; -.
DR PRIDE; P37534; -.
DR EnsemblBacteria; CAB11800; CAB11800; BSU_00240.
DR GeneID; 937016; -.
DR KEGG; bsu:BSU00240; -.
DR PATRIC; fig|224308.179.peg.24; -.
DR eggNOG; ENOG5033CHE; Bacteria.
DR OMA; DAKYHFF; -.
DR BioCyc; BSUB:BSU00240-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR019700; Sigma-G_inhibitor_Gin.
DR Pfam; PF10764; Gin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Reference proteome; Sporulation;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..64
FT /note="Anti-sigma-G factor Gin"
FT /id="PRO_0000079393"
FT BINDING 11
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:19497328"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:19497328"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:19497328"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:19497328"
FT MUTAGEN 11..14
FT /note="CVIC->AVIA: No longer inhibits sigma-G. Restores 70%
FT of sigma-G inhibition; when associated with 30-A--A-33."
FT /evidence="ECO:0000269|PubMed:19497328"
FT MUTAGEN 11
FT /note="C->A: No longer inhibits sigma-G."
FT /evidence="ECO:0000269|PubMed:19497328"
FT MUTAGEN 14
FT /note="C->A: No longer inhibits or interacts with sigma-G."
FT /evidence="ECO:0000269|PubMed:19497328"
FT MUTAGEN 15..32
FT /note="DQEKNRGIHLYTKFICLD->RKPLKDGIIINGKGICKS: Loss of most
FT ability to inhibit sigma-G, no longer interacts with sigma-
FT G, replace sequence with same region from
FT C.acetobutylicum."
FT /evidence="ECO:0000269|PubMed:18208527"
FT MUTAGEN 21
FT /note="G->C: Loss of most sigma-G inhibition."
FT /evidence="ECO:0000269|PubMed:19497328"
FT MUTAGEN 30..33
FT /note="CLDC->ALDA: No longer inhibits sigma-G. Restores 70%
FT of sigma-G inhibition; when associated with 11-A--A-14."
FT /evidence="ECO:0000269|PubMed:19497328"
FT MUTAGEN 30
FT /note="C->A: No longer inhibits sigma-G."
FT /evidence="ECO:0000269|PubMed:19497328"
FT MUTAGEN 33
FT /note="C->A: No longer inhibits or interacts with sigma-G."
FT /evidence="ECO:0000269|PubMed:19497328"
FT MUTAGEN 47
FT /note="Y->A: No longer inhibits or interacts with sigma-G."
FT /evidence="ECO:0000269|PubMed:19497328"
FT MUTAGEN 49..50
FT /note="FY->AA: No longer inhibits sigma-G, still slight
FT interaction with sigma-G."
FT /evidence="ECO:0000269|PubMed:19497328"
FT MUTAGEN 50
FT /note="Y->A: Partial loss of sigma-G inhibition."
FT /evidence="ECO:0000269|PubMed:19497328"
FT MUTAGEN 51
FT /note="V->A: Loss of most sigma-G inhibition, still slight
FT interaction with sigma-G."
FT /evidence="ECO:0000269|PubMed:19497328"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:5N7Y"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:5N7Y"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:5N7Y"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:5N7Y"
FT HELIX 31..40
FT /evidence="ECO:0007829|PDB:5N7Y"
SQ SEQUENCE 64 AA; 7439 MW; C423AA65E835E8F5 CRC64;
MDETVKLNHT CVICDQEKNR GIHLYTKFIC LDCERKVIST STSDPDYAFY VKKLKSIHTP
PLYS
